Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms Journal Article
| Authors: | Jeffrey, P. D.; Gorina, S.; Pavletich, N. P. |
| Article Title: | Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms |
| Abstract: | The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a β strand and an α helix, associates with a second monomer across an antiparallel β sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer. |
| Keywords: | protein domain; transcription factor; protein p53; tumor suppressor gene; cell transformation; polymerization; crystal structure; carcinoma cell; oligomer; priority journal; article |
| Journal Title: | Science |
| Volume: | 267 |
| Issue: | 5203 |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Date Published: | 1995-03-10 |
| Start Page: | 1498 |
| End Page: | 1502 |
| Language: | English |
| DOI: | 10.1126/science.7878469 |
| PUBMED: | 7878469 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 28 August 2018 -- Source: Scopus |
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